ID   SLP1_SCHPO              Reviewed;         488 AA.
AC   P78972;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=WD repeat-containing protein slp1;
GN   Name=slp1; ORFNames=SPAC821.08c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9001228; DOI=10.1128/mcb.17.2.742;
RA   Matsumoto T.;
RT   "A fission yeast homolog of CDC20/p55CDC/Fizzy is required for recovery
RT   from DNA damage and genetically interacts with p34cdc2.";
RL   Mol. Cell. Biol. 17:742-750(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF 131-ALA-PHE-132.
RX   PubMed=9461438; DOI=10.1126/science.279.5353.1045;
RA   Kim S.H., Lin D.P., Matsumoto S., Kitazono A., Matsumoto T.;
RT   "Fission yeast Slp1: an effector of the Mad2-dependent spindle
RT   checkpoint.";
RL   Science 279:1045-1047(1998).
RN   [4]
RP   INTERACTION WITH MAD3.
RX   PubMed=11909965; DOI=10.1128/mcb.22.8.2728-2742.2002;
RA   Millband D.N., Hardwick K.G.;
RT   "Fission yeast Mad3p is required for Mad2p to inhibit the anaphase-
RT   promoting complex and localizes to kinetochores in a Bub1p-, Bub3p-, and
RT   Mph1p-dependent manner.";
RL   Mol. Cell. Biol. 22:2728-2742(2002).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH MES1 AND CDC13.
RX   PubMed=15791259; DOI=10.1038/nature03406;
RA   Izawa D., Goto M., Yamashita A., Yamano H., Yamamoto M.;
RT   "Fission yeast Mes1p ensures the onset of meiosis II by blocking
RT   degradation of cyclin Cdc13p.";
RL   Nature 434:529-533(2005).
CC   -!- FUNCTION: Required for mad2-dependent spindle checkpoint activation.
CC       Promotes ubiquitin-dependent degradation of cdc13 by the anaphase
CC       promoting complex/cyclosome (APC/C). {ECO:0000269|PubMed:15791259,
CC       ECO:0000269|PubMed:9001228, ECO:0000269|PubMed:9461438}.
CC   -!- SUBUNIT: Interacts with cdc13, mad3 and mes1.
CC       {ECO:0000269|PubMed:11909965, ECO:0000269|PubMed:15791259}.
CC   -!- INTERACTION:
CC       P78972; O14417: mad2; NbExp=8; IntAct=EBI-1252744, EBI-1269310;
CC       P78972; P41005: mes1; NbExp=2; IntAct=EBI-1252744, EBI-1553555;
CC   -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR   EMBL; U77983; AAC49621.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB57442.1; -; Genomic_DNA.
DR   PIR; T41719; T41719.
DR   RefSeq; NP_593161.1; NM_001018559.2.
DR   PDB; 4AEZ; X-ray; 2.30 A; A/D/G=88-488.
DR   PDBsum; 4AEZ; -.
DR   AlphaFoldDB; P78972; -.
DR   SMR; P78972; -.
DR   BioGRID; 279650; 30.
DR   ComplexPortal; CPX-3924; Mitotic Checkpoint Complex.
DR   ComplexPortal; CPX-764; Anaphase-Promoting Complex variant 2.
DR   DIP; DIP-38036N; -.
DR   ELM; P78972; -.
DR   IntAct; P78972; 4.
DR   STRING; 284812.P78972; -.
DR   iPTMnet; P78972; -.
DR   PaxDb; 4896-SPAC821-08c-1; -.
DR   EnsemblFungi; SPAC821.08c.1; SPAC821.08c.1:pep; SPAC821.08c.
DR   GeneID; 2543222; -.
DR   KEGG; spo:SPAC821.08c; -.
DR   PomBase; SPAC821.08c; slp1.
DR   VEuPathDB; FungiDB:SPAC821.08c; -.
DR   eggNOG; KOG0305; Eukaryota.
DR   HOGENOM; CLU_014831_6_0_1; -.
DR   InParanoid; P78972; -.
DR   OMA; CSGACLN; -.
DR   PhylomeDB; P78972; -.
DR   Reactome; R-SPO-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR   Reactome; R-SPO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-SPO-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P78972; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0000776; C:kinetochore; NAS:ComplexPortal.
DR   GO; GO:0033597; C:mitotic checkpoint complex; IDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IPI:PomBase.
DR   GO; GO:1990757; F:ubiquitin ligase activator activity; IDA:PomBase.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990949; P:metaphase/anaphase transition of meiosis I; EXP:PomBase.
DR   GO; GO:1990950; P:metaphase/anaphase transition of meiosis II; EXP:PomBase.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; NAS:ComplexPortal.
DR   GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; NAS:PomBase.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19918; CELL DIVISION CYCLE 20 CDC20 FIZZY -RELATED; 1.
DR   PANTHER; PTHR19918:SF68; FI02843P; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Mitosis; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..488
FT                   /note="WD repeat-containing protein slp1"
FT                   /id="PRO_0000051220"
FT   REPEAT          178..215
FT                   /note="WD 1"
FT   REPEAT          219..258
FT                   /note="WD 2"
FT   REPEAT          261..298
FT                   /note="WD 3"
FT   REPEAT          302..341
FT                   /note="WD 4"
FT   REPEAT          344..386
FT                   /note="WD 5"
FT   REPEAT          388..429
FT                   /note="WD 6"
FT   REPEAT          434..473
FT                   /note="WD 7"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         131..132
FT                   /note="AF->PY: Abrogates binding to mad2 and overrides
FT                   activation of the spindle checkpoint by mad2."
FT                   /evidence="ECO:0000269|PubMed:9461438"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          192..198
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          233..240
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          245..249
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          255..259
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          266..272
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          275..280
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          283..289
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          307..312
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          316..323
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          336..342
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          351..354
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          361..365
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   TURN            368..370
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          372..377
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          383..388
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          393..398
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          400..409
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   TURN            411..413
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          415..422
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          425..433
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          448..454
FT                   /evidence="ECO:0007829|PDB:4AEZ"
FT   STRAND          458..464
FT                   /evidence="ECO:0007829|PDB:4AEZ"
SQ   SEQUENCE   488 AA;  53418 MW;  52E021FD4EECE5DE CRC64;
     MEIAGNSSTI SPTFSTPTKK RNLVFPNSPI TPLHQQALLG RNGRSSKRCS PKSSFIRNSP
     KIDVVNTDWS IPLCGSPRNK SRPASRSDRF IPSRPNTANA FVNSISSDVP FDYSESVAEA
     CGFDLNTRVL AFKLDAPEAK KPVDLRTQHN RPQRPVVTPA KRRFNTTPER VLDAPGIIDD
     YYLNLLDWSN LNVVAVALER NVYVWNADSG SVSALAETDE STYVASVKWS HDGSFLSVGL
     GNGLVDIYDV ESQTKLRTMA GHQARVGCLS WNRHVLSSGS RSGAIHHHDV RIANHQIGTL
     QGHSSEVCGL AWRSDGLQLA SGGNDNVVQI WDARSSIPKF TKTNHNAAVK AVAWCPWQSN
     LLATGGGTMD KQIHFWNAAT GARVNTVDAG SQVTSLIWSP HSKEIMSTHG FPDNNLSIWS
     YSSSGLTKQV DIPAHDTRVL YSALSPDGRI LSTAASDENL KFWRVYDGDH VKRPIPITKT
     PSSSITIR
//